Aliases for CYP1A2 Gene
External Ids for CYP1A2 Gene
Previous GeneCards Identifiers for CYP1A2 Gene
This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. The protein encoded by this gene localizes to the endoplasmic reticulum and its expression is induced by some polycyclic aromatic hydrocarbons (PAHs), some of which are found in cigarette smoke. The enzyme's endogenous substrate is unknown; however, it is able to metabolize some PAHs to carcinogenic intermediates. Other xenobiotic substrates for this enzyme include caffeine, aflatoxin B1, and acetaminophen. The transcript from this gene contains four Alu sequences flanked by direct repeats in the 3' untranslated region. [provided by RefSeq, Jul 2008]
GeneCards Summary for CYP1A2 Gene
CYP1A2 (Cytochrome P450, Family 1, Subfamily A, Polypeptide 2) is a Protein Coding gene. Diseases associated with CYP1A2 include toxicity or absent response to clozapine and cyp1a2-related altered drug metabolism. Among its related pathways are Platelet Aggregation Inhibitor Pathway, Pharmacodynamics and AhR pathway (WikiPathways). GO annotations related to this gene include enzyme binding and iron ion binding. An important paralog of this gene is CYP21A2.
UniProtKB/Swiss-Prot for CYP1A2 Gene
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Most active in catalyzing 2-hydroxylation. Caffeine is metabolized primarily by cytochrome CYP1A2 in the liver through an initial N3-demethylation. Also acts in the metabolism of aflatoxin B1 and acetaminophen. Participates in the bioactivation of carcinogenic aromatic and heterocyclic amines. Catalizes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin.